Purification and Characterization of a Monohalomethane-producing Enzyme S-adenosyl-L-methionine : Halide Ion Methyltransferase from a Marine Microalga, Pavlova pinguis(Biochemistry & Molecular Biology)

概要

論文の詳細を見る
A monohalomethane-producing enzyme, S-adenosyl-L-methionine-dependent halide ion methyltransferase (EC 2.1.1.-) was purified from the marine microalga Pavlova pinguis by two anion exchange, hydroxyapatite and gel filtration chromatographies. The methyltransferase was a monomeric molecule having a molecular weight of 29,000. The enzyme had an isoelectric point at 5.3, and was optimally active at pH 8.0. The K_m for iodide and SAM were 12 mм and 12μм, respectively, which were measured using a partially purified enzyme. Various metal ions had no significant effect on methyl iodide production, suggesting that the enzyme does not require metal ions. The enzyme reaction strictly depended on SAM as a methyl donor, and the enzyme catalyzed methylation of the I^-, Br^-, and Cl^- to corresponding monohalomethanes and of bisulfide to methyl mercaptan.
社団法人日本農芸化学会の論文
2001-11-23